Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aspartate aminotransferase, mitochondrial  

UniProtKB / Swiss-Prot ID :  AATM_MOUSE

Gene Name (Synonyms) : 
Got2, Got-2  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Mitochondrion matrix. Cell membrane. 

Protein Function :  Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. 

Protein Sequence MALLHSSRILSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDD...
Predicted Secondary Structure CCEEECCCEEECCCHHCCCCCCCCCCCCCHHHHHCCCCCCCCCHHHHHHHHHHHCCCCCCEEEECCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
67PhosphotyrosineGVGAYRDDN
EECCCCCCC
14.51Phosphositeplus
Link
73N6-acetyllysineDDNGKPYVL
CCCCCCCCC
39.16Phosphositeplus
Link
94N6-acetyllysineKNLDKEYLP
CCCCCCCCC
51.96Phosphositeplus
Link
94N6-acetyllysine.KNLDKEYLP
CCCCCCCCC
51.96UniProtKB
Link
96Nitrated tyrosine.LDKEYLPIG
CCCCCCCCC
24.42UniProtKB
Link
96PhosphotyrosineLDKEYLPIG
CCCCCCCCC
24.42Phosphositeplus
Link
96PhosphotyrosineLDKEYLPIG
CCCCCCCCC
24.42SysPTM
Link
106S-nitrosocysteineLAEFCKASA
HHHHHHHHH
2.44dbSNO
Link
133PhosphoserineVQTISGTGA
EEEEECCCH
33.42Phosphositeplus
Link
143PhosphoserineRVGASFLQR
HHHHHHHHH
22.14Phosphositeplus
Link
150N6-acetyllysineQRFFKFSRD
HHHCCCCCE
39.45Phosphositeplus
Link
159N6-acetyllysineVFLPKPSWG
EEEECCCCC
54.56Phosphositeplus
Link
159N6-acetyllysine.VFLPKPSWG
EEEECCCCC
54.56UniProtKB
Link
166PhosphothreonineWGNHTPIFR
CCCHHHHHH
23.29Phosphositeplus
Link
185N6-acetyllysineYYDPKTCGF
EEECCCCCC
54.25Phosphositeplus
Link
185N6-acetyllysine.YYDPKTCGF
EEECCCCCC
54.25UniProtKB
Link
187S-nitrosocysteineDPKTCGFDF
ECCCCCCCH
6.80dbSNO
Link
212S-nitrosocysteineLLHACAHNP
EEEECCCCC
2.49dbSNO
Link
295S-nitrosocysteineFTVVCKDAE
HHHCCCCHH
2.61dbSNO
Link
296N6-acetyllysineTVVCKDAEE
HHCCCCHHH
48.65Phosphositeplus
Link
296N6-acetyllysine.TVVCKDAEE
HHCCCCHHH
48.65UniProtKB
Link
302N6-acetyllysineAEEAKRVES
HHHHHHHHH
61.32Phosphositeplus
Link
309N6-acetyllysineESQLKILIR
HHHHHHHHH
28.03Phosphositeplus
Link
333PhosphoserineTILTSPDLR
HHCCCHHHH
16.99Phosphositeplus
Link
345N6-acetyllysineLQEVKGMAD
HHHHHHHHH
42.06Phosphositeplus
Link
345N6-acetyllysine.LQEVKGMAD
HHHHHHHHH
42.06UniProtKB
Link
363N6-acetyllysineVSNLKKEGS
HHHHHHCCC
53.69Phosphositeplus
Link
363N6-acetyllysine.VSNLKKEGS
HHHHHHCCC
53.69UniProtKB
Link
382S-nitrosocysteineIGMFCFTGL
CCCEEECCC
1.90dbSNO
Link
404N6-acetyllysineVYMTKDGRI
EEECCCCEE
41.47Phosphositeplus
Link
430N6-acetyllysineHQVTK
HHHHC
60.53Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-159; LYS-185;LYS-296; LYS-345 AND LYS-363, AND MASS SPECTROMETRY.
Nitration
ReferencePubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease.";
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.;
Biochemistry 45:8009-8022(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures